Overview
| Uniprot ID | Q4KMA2 |
|---|
| Protein Name | Lysine-specific demethylase RAD23B |
|---|
| Gene Name | Rad23b |
|---|
| Organism | Rattus norvegicus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 45 |
AFPVAGQKLIYAGKI |
Function
Multifunctional protein that participates in histone H4K20 demethylation, DNA repair, ubiquitin-dependent protein degradation and transcriptional regulation. Specifically demethylates mono-, di- and trimethylated 'Lys-20' of histone H4 (H4K20me1, H4K20me2, H4K20me3, respectively) into unmethylated forms. Activates the transcription of coding genes by demethylating H4K20me1 and the transcription of repetitive elements by demethylating H4K20me3. Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex, a nucleotide-excision repair complex that is involved in damage sensing during global genome nucleotide excision repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA. Recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix including single-stranded loops, mismatched bubbles or single-stranded overhangs. Cooperatively with CETN2 appears to stabilize XPC
Protein Sequence
10
MQVTLKTLQQ
20
QTFKIDIDPE
30
ETVKALKEKI
40
ESEKGKDAFP
50
VAGQKLIYAG
60
KILSDDTALK
70
EYKIDEKNFV
80
VVMVTKPKAV
90
TSAVPATTQQ
100
SSSPSTTTVS
110
SSPAAAVAQA
120
PAPTPALAPT
130
STPASTTPAS
140
TTASSEPAPT
150
GATQPEKPAE
160
KPAQTPVLTS
170
PAPADSTPGD
180
SSRSNLFEDA
190
TSALVTGQSY
200
ENMVTEIMSM
210
GYEREQVIAA
220
LRASFNNPDR
230
AVEYLLMGIP
240
GDRESQAVVD
250
PPPQAVSTGT
260
PQSPAVAAAA
270
ATTTATTTTT
280
SGGHPLEFLR
290
NQPQFQQMRQ
300
IIQQNPSLLP
310
ALLQQIGREN
320
PQLLQQISQH
330
QEHFIQMLNE
340
PVQEAGGQGG
350
GGGGGGGGGG
360
GGGGIAEAGS
370
GHMNYIQVTP
380
QEKEAIERLK
390
ALGFPEGLVI
400
QAYFACEKNE
410
NLAANFLLQQ
NFDED
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0000502 |
proteasome complex |
| Cellular Component |
GO:0071942 |
XPC complex |
| Molecular Function |
GO:0003684 |
damaged DNA binding |
| Molecular Function |
GO:0140612 |
DNA damage sensor activity |
| Molecular Function |
GO:0035575 |
histone H4K20 demethylase activity |
| Molecular Function |
GO:0031593 |
polyubiquitin modification-dependent protein binding |
| Molecular Function |
GO:0070628 |
proteasome binding |
| Molecular Function |
GO:0000978 |
RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| Molecular Function |
GO:0061629 |
RNA polymerase II-specific DNA-binding transcription factor binding |
| Molecular Function |
GO:0000976 |
transcription cis-regulatory region binding |
| Molecular Function |
GO:0043130 |
ubiquitin binding |
| Biological Process |
GO:0098761 |
cellular response to interleukin-7 |
| Biological Process |
GO:0006974 |
DNA damage response |
| Biological Process |
GO:0048568 |
embryonic organ development |
| Biological Process |
GO:0006289 |
nucleotide-excision repair |
| Biological Process |
GO:0043161 |
proteasome-mediated ubiquitin-dependent protein catabolic process |
| Biological Process |
GO:0032434 |
regulation of proteasomal ubiquitin-dependent protein catabolic process |
| Biological Process |
GO:0007283 |
spermatogenesis |
Reference
[1] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.